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Q9UBS8

- RNF14_HUMAN

UniProt

Q9UBS8 - RNF14_HUMAN

Protein

E3 ubiquitin-protein ligase RNF14

Gene

RNF14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Might act as an E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates, which could be nuclear proteins. Could play a role as a coactivator for androgen- and, to a lesser extent, progesterone-dependent transcription.1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri220 – 27051RING-type 1; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri289 – 35062IBR-typeAdd
    BLAST
    Zinc fingeri404 – 43330RING-type 2; degeneratePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. small conjugating protein ligase activity Source: UniProtKB
    4. transcription coactivator activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. positive regulation of transcription, DNA-templated Source: UniProtKB
    3. protein ubiquitination Source: UniProtKB
    4. regulation of androgen receptor signaling pathway Source: UniProtKB
    5. regulation of transcription, DNA-templated Source: UniProtKB
    6. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. response to estradiol Source: BHF-UCL
    8. signal transduction Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase RNF14 (EC:6.3.2.-)
    Alternative name(s):
    Androgen receptor-associated protein 54
    HFB30
    RING finger protein 14
    Triad2 protein
    Gene namesi
    Name:RNF14
    Synonyms:ARA54
    ORF Names:HRIHFB2038
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:10058. RNF14.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi220 – 2201C → S: Loss of interaction with UBE2E2 and of autoubiquitination. 1 Publication

    Organism-specific databases

    PharmGKBiPA34423.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 474474E3 ubiquitin-protein ligase RNF14PRO_0000056057Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei348 – 3481Phosphoserine1 Publication

    Post-translational modificationi

    RING-type zinc finger-dependent and UBE2E2-dependent autoubiquitination.

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UBS8.
    PaxDbiQ9UBS8.
    PRIDEiQ9UBS8.

    PTM databases

    PhosphoSiteiQ9UBS8.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiQ9UBS8.
    BgeeiQ9UBS8.
    CleanExiHS_RNF14.
    GenevestigatoriQ9UBS8.

    Organism-specific databases

    HPAiHPA008716.

    Interactioni

    Subunit structurei

    Interacts with the ubiquitin-conjugating enzymes UBE2E1 and UBE2E2. Interacts with AR/androgen receptor; testosterone- and RNF6-regulated it promotes AR transcriptional activity.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102752EBI-2130308,EBI-608057

    Protein-protein interaction databases

    BioGridi114968. 21 interactions.
    IntActiQ9UBS8. 16 interactions.
    MINTiMINT-1187964.
    STRINGi9606.ENSP00000324956.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UBS8.
    SMRiQ9UBS8. Positions 188-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 137127RWDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni361 – 474114Interaction with androgen receptorAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili351 – 39545Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi37 – 459D-box

    Domaini

    The N-terminal destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway.By similarity
    The RING-type zinc finger is essential for the interaction with UBE2E2.

    Sequence similaritiesi

    Belongs to the RBR family. RNF14 subfamily.Curated
    Contains 1 IBR-type zinc finger.Curated
    Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 RWD domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri220 – 27051RING-type 1; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri289 – 35062IBR-typeAdd
    BLAST
    Zinc fingeri404 – 43330RING-type 2; degeneratePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG266709.
    HOVERGENiHBG057296.
    InParanoidiQ9UBS8.
    KOiK11971.
    OMAiQYFCWLC.
    PhylomeDBiQ9UBS8.
    TreeFamiTF314401.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR006575. RWD-domain.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    IPR002867. Znf_C6HC.
    IPR001841. Znf_RING.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF01485. IBR. 2 hits.
    PF05773. RWD. 1 hit.
    [Graphical view]
    SMARTiSM00647. IBR. 2 hits.
    SM00184. RING. 1 hit.
    SM00591. RWD. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS50908. RWD. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBS8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSSEDREAQE DELLALASIY DGDEFRKAES VQGGETRIYL DLPQNFKIFV    50
    SGNSNECLQN SGFEYTICFL PPLVLNFELP PDYPSSSPPS FTLSGKWLSP 100
    TQLSALCKHL DNLWEEHRGS VVLFAWMQFL KEETLAYLNI VSPFELKIGS 150
    QKKVQRRTAQ ASPNTELDFG GAAGSDVDQE EIVDERAVQD VESLSNLIQE 200
    ILDFDQAQQI KCFNSKLFLC SICFCEKLGS ECMYFLECRH VYCKACLKDY 250
    FEIQIRDGQV QCLNCPEPKC PSVATPGQVK ELVEAELFAR YDRLLLQSSL 300
    DLMADVVYCP RPCCQLPVMQ EPGCTMGICS SCNFAFCTLC RLTYHGVSPC 350
    KVTAEKLMDL RNEYLQADEA NKRLLDQRYG KRVIQKALEE MESKEWLEKN 400
    SKSCPCCGTP IEKLDGCNKM TCTGCMQYFC WICMGSLSRA NPYKHFNDPG 450
    SPCFNRLFYA VDVDDDIWED EVED 474
    Length:474
    Mass (Da):53,837
    Last modified:May 1, 2000 - v1
    Checksum:i529E3F5AF38A5DAD
    GO
    Isoform 2 (identifier: Q9UBS8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-126: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:348
    Mass (Da):39,634
    Checksum:iC43770874596DD0C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 321Q → R in CAG32983. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 126126Missing in isoform 2. 1 PublicationVSP_045780Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB022663 mRNA. Translation: BAA78677.1.
    AF060544 mRNA. Translation: AAD21842.1.
    AK023884 mRNA. Translation: BAG51234.1.
    AK057868 mRNA. No translation available.
    CR456702 mRNA. Translation: CAG32983.1.
    AC005740 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61895.1.
    CH471062 Genomic DNA. Translation: EAW61896.1.
    CH471062 Genomic DNA. Translation: EAW61897.1.
    BC126185 mRNA. Translation: AAI26186.1.
    BC144061 mRNA. Translation: AAI44062.1.
    AB015333 mRNA. Translation: BAA34792.1.
    CCDSiCCDS4270.1. [Q9UBS8-1]
    CCDS4271.1. [Q9UBS8-2]
    RefSeqiNP_001188294.1. NM_001201365.1. [Q9UBS8-1]
    NP_004281.1. NM_004290.4. [Q9UBS8-1]
    NP_899645.1. NM_183398.2. [Q9UBS8-2]
    NP_899646.1. NM_183399.2. [Q9UBS8-1]
    NP_899647.1. NM_183400.2. [Q9UBS8-1]
    NP_899648.1. NM_183401.2. [Q9UBS8-1]
    XP_005268593.1. XM_005268536.1. [Q9UBS8-1]
    XP_005268594.1. XM_005268537.1. [Q9UBS8-1]
    XP_005268595.1. XM_005268538.1. [Q9UBS8-1]
    XP_005268596.1. XM_005268539.1. [Q9UBS8-2]
    XP_005268597.1. XM_005268540.1. [Q9UBS8-2]
    XP_005268598.1. XM_005268541.1. [Q9UBS8-2]
    UniGeneiHs.483616.

    Genome annotation databases

    EnsembliENST00000347642; ENSP00000324956; ENSG00000013561. [Q9UBS8-1]
    ENST00000356143; ENSP00000348462; ENSG00000013561. [Q9UBS8-1]
    ENST00000394514; ENSP00000378022; ENSG00000013561. [Q9UBS8-2]
    ENST00000394519; ENSP00000378027; ENSG00000013561. [Q9UBS8-1]
    ENST00000394520; ENSP00000378028; ENSG00000013561. [Q9UBS8-1]
    GeneIDi9604.
    KEGGihsa:9604.
    UCSCiuc003lly.3. human. [Q9UBS8-1]

    Polymorphism databases

    DMDMi17380293.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB022663 mRNA. Translation: BAA78677.1 .
    AF060544 mRNA. Translation: AAD21842.1 .
    AK023884 mRNA. Translation: BAG51234.1 .
    AK057868 mRNA. No translation available.
    CR456702 mRNA. Translation: CAG32983.1 .
    AC005740 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61895.1 .
    CH471062 Genomic DNA. Translation: EAW61896.1 .
    CH471062 Genomic DNA. Translation: EAW61897.1 .
    BC126185 mRNA. Translation: AAI26186.1 .
    BC144061 mRNA. Translation: AAI44062.1 .
    AB015333 mRNA. Translation: BAA34792.1 .
    CCDSi CCDS4270.1. [Q9UBS8-1 ]
    CCDS4271.1. [Q9UBS8-2 ]
    RefSeqi NP_001188294.1. NM_001201365.1. [Q9UBS8-1 ]
    NP_004281.1. NM_004290.4. [Q9UBS8-1 ]
    NP_899645.1. NM_183398.2. [Q9UBS8-2 ]
    NP_899646.1. NM_183399.2. [Q9UBS8-1 ]
    NP_899647.1. NM_183400.2. [Q9UBS8-1 ]
    NP_899648.1. NM_183401.2. [Q9UBS8-1 ]
    XP_005268593.1. XM_005268536.1. [Q9UBS8-1 ]
    XP_005268594.1. XM_005268537.1. [Q9UBS8-1 ]
    XP_005268595.1. XM_005268538.1. [Q9UBS8-1 ]
    XP_005268596.1. XM_005268539.1. [Q9UBS8-2 ]
    XP_005268597.1. XM_005268540.1. [Q9UBS8-2 ]
    XP_005268598.1. XM_005268541.1. [Q9UBS8-2 ]
    UniGenei Hs.483616.

    3D structure databases

    ProteinModelPortali Q9UBS8.
    SMRi Q9UBS8. Positions 188-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114968. 21 interactions.
    IntActi Q9UBS8. 16 interactions.
    MINTi MINT-1187964.
    STRINGi 9606.ENSP00000324956.

    PTM databases

    PhosphoSitei Q9UBS8.

    Polymorphism databases

    DMDMi 17380293.

    Proteomic databases

    MaxQBi Q9UBS8.
    PaxDbi Q9UBS8.
    PRIDEi Q9UBS8.

    Protocols and materials databases

    DNASUi 9604.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000347642 ; ENSP00000324956 ; ENSG00000013561 . [Q9UBS8-1 ]
    ENST00000356143 ; ENSP00000348462 ; ENSG00000013561 . [Q9UBS8-1 ]
    ENST00000394514 ; ENSP00000378022 ; ENSG00000013561 . [Q9UBS8-2 ]
    ENST00000394519 ; ENSP00000378027 ; ENSG00000013561 . [Q9UBS8-1 ]
    ENST00000394520 ; ENSP00000378028 ; ENSG00000013561 . [Q9UBS8-1 ]
    GeneIDi 9604.
    KEGGi hsa:9604.
    UCSCi uc003lly.3. human. [Q9UBS8-1 ]

    Organism-specific databases

    CTDi 9604.
    GeneCardsi GC05P141358.
    HGNCi HGNC:10058. RNF14.
    HPAi HPA008716.
    MIMi 605675. gene.
    neXtProti NX_Q9UBS8.
    PharmGKBi PA34423.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266709.
    HOVERGENi HBG057296.
    InParanoidi Q9UBS8.
    KOi K11971.
    OMAi QYFCWLC.
    PhylomeDBi Q9UBS8.
    TreeFami TF314401.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi RNF14. human.
    GeneWikii RNF14.
    GenomeRNAii 9604.
    NextBioi 36027.
    PROi Q9UBS8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBS8.
    Bgeei Q9UBS8.
    CleanExi HS_RNF14.
    Genevestigatori Q9UBS8.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR006575. RWD-domain.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    IPR002867. Znf_C6HC.
    IPR001841. Znf_RING.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF01485. IBR. 2 hits.
    PF05773. RWD. 1 hit.
    [Graphical view ]
    SMARTi SM00647. IBR. 2 hits.
    SM00184. RING. 1 hit.
    SM00591. RWD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS50908. RWD. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a novel human gene (HFB30) which encodes a protein with a RING finger motif."
      Ueki N., Seki N., Yano K., Masuho Y., Saito T., Muramatsu M.-A.
      Biochim. Biophys. Acta 1445:232-236(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "Cloning and characterization of human prostate coactivator ARA54, a novel protein that associates with the androgen receptor."
      Kang H.-Y., Yeh S., Fujimoto N., Chang C.
      J. Biol. Chem. 274:8570-8576(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
      Tissue: Prostate.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain and Thyroid.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "Selection system for genes encoding nuclear-targeted proteins."
      Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
      Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-474 (ISOFORM 1), SUBCELLULAR LOCATION.
      Tissue: Fetal brain.
    9. "N-terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8."
      Ito K., Adachi S., Iwakami R., Yasuda H., Muto Y., Seki N., Okano Y.
      Eur. J. Biochem. 268:2725-2732(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-220.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Regulation of androgen receptor transcriptional activity and specificity by RNF6-induced ubiquitination."
      Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z., Chen H., Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z., Veenstra T.D., Qiu Y.
      Cancer Cell 15:270-282(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AR.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    Entry informationi

    Entry nameiRNF14_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBS8
    Secondary accession number(s): A0AV26
    , A6NMR2, A8MTW5, B3KN72, B7ZLV2, D3DQE4, O94793, Q6IBV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3